dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001156_02120

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Basic Information help

Species

SFHK01 sp004556395

Lineage

Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; SFHK01; SFHK01 sp004556395

CAZyme ID

MGYG000001156_02120

CAZy Family

GH36

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
536	MGYG000001156_110\|CGC1	60243.12	5.2604

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001156	2933732	MAG	Austria	Europe

Gene Location

Start: 2357; End: 3967 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001156_02120.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14791	GH36	4.49e-34	195	489	2	296	glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
COG3345	GalA	3.81e-11	183	446	280	570	Alpha-galactosidase [Carbohydrate transport and metabolism].
cd14790	GH_D	9.62e-09	236	443	39	206	Glycoside hydrolases, clan D. This group of glycosyl hydrolase families is comprised of glycosyl hydrolase family 31 (GH31), family 36 (GH36), and family 27 (GH27). These structurally and mechanistically related protein families are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively. They have a wide range of functions including alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase, alpha-N-acetylgalactosaminidase, stachyose synthase, raffinose synthase, and alpha-1,4-glucan lyase.
cd14792	GH27	1.23e-06	235	483	41	260	glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCU01578.1	1.40e-163	5	532	30	549
CBL19648.1	1.99e-163	5	532	30	549
SNU96820.1	1.98e-159	4	525	9	525
QIB59833.1	4.02e-157	27	525	34	528
BDA09953.1	2.28e-156	27	525	34	528

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5M0X_A	4.06e-09	185	446	196	457	Structureof apo structure of GH36 alpha-galactosidase from Thermotoga maritima [Thermotoga maritima],5M12_A Structure of GH36 alpha-galactosidase from Thermotoga maritima in complex with intact cyclopropyl-carbasugar. [Thermotoga maritima],5M16_A Structure of GH36 alpha-galactosidase from Thermotoga maritima in complex with a hydrolysed cyclopropyl carbasugar. [Thermotoga maritima],5M1I_A Structure of GH36 alpha-galactosidase from Thermotoga maritima in a covalent complex with a cyclopropyl carbasugar. [Thermotoga maritima],6GVD_A Alpha-galactosidase from Thermotoga maritima in complex with cyclohexene-based carbasugar mimic of galactose [Thermotoga maritima MSB8],6GWG_A Alpha-galactosidase from Thermotoga maritima in complex with cyclohexene-based carbasugar mimic of galactose covalently linked to the nucleophile [Thermotoga maritima MSB8],6GX8_A Alpha-galactosidase from Thermotoga maritima in complex with hydrolysed cyclohexene-based carbasugar mimic of galactose [Thermotoga maritima MSB8]
1ZY9_A	2.81e-08	189	446	189	446	Crystalstructure of Alpha-galactosidase (EC 3.2.1.22) (Melibiase) (tm1192) from Thermotoga maritima at 2.34 A resolution [Thermotoga maritima]
6GTA_A	2.84e-08	185	446	196	457	Alpha-galactosidasemutant D378A from Thermotoga maritima in complex with intact cyclohexene-based carbasugar mimic of galactose with 3,5 difluorophenyl leaving group [Thermotoga maritima MSB8],6GWF_A Alpha-galactosidase mutant D387A from Thermotoga maritima in complex with intact cyclohexene-based carbasugar mimic of galactose with 2,4-dinitro leaving group [Thermotoga maritima MSB8]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
G4FEF4	2.16e-08	185	446	173	434	Alpha-galactosidase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=galA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000041	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000001156_02120.